Table 2.
Ranking of MVH residues showing strongly attractive interactions with the three receptors. (a) SLAM; (b) Nectin-4; (c) CD46.
| Rank | (a) SLAM (Chain B in PDB Code 3ALZ) | ||||
|---|---|---|---|---|---|
| MVH Amino Acid (a.a.) Position (1) | IFIE Sum (2) with the Receptor | Receptor a.a. with the Highest (1st) Affinity (3) | IFIE-1st (4) with the Receptor a.a. | IFIE-1st/IFIE Sum Ratio (5) | |
| (kcal/mol) | (kcal/mol) | ||||
| 1 | Asp507(−) | −133.2 | Lys77(+) | −80.0 | 60% |
| 2 | Asp505(−) | −107.7 | Lys77(+) | −106.3 | 99% |
| 3 | Arg533(+) | −80.5 | Glu123(−) | −122.0 | 152% |
| 4 | Arg556(+) | −74.2 | Glu123(−) | −45.7 | 62% |
| 5 | Asp530(−) | −67.6 | Lys77(+) | −66.4 | 98% |
| 6 | Glu503(−) | −53.4 | Lys77(+) | −48.0 | 90% |
| 7 | Arg195(+) | −36.7 | Ser127 | −24.9 | 68% |
| 8 | Thr193(*) | −32.6 | Arg130(+) | −15.3 | 47% |
| 9 | Phe552(*) | −18.6 | Glu 75(−) | −9.2 | 49% |
| 10 | Tyr551(*) | −18.0 | Arg130(+) | −17.8 | 99% |
| 11 | Tyr553(*) | −14.1 | Ser 127 | −7.2 | 51% |
| 12 | Ser532(*) | −13.1 | Ser 80 | −4.8 | 37% |
| 13 | Phe483(*) | −12.3 | Asn72 | −11.8 | 96% |
| 14 | Gly196(*) | −9.3 | Ser 127 | −11.7 | 126% |
| 15 | Pro554 | −8.9 | Glu123(−) | −9.9 | 111% |
| 16 | Tyr541(*) | −8.6 | Glu 75(−) | −6.3 | 73% |
| 17 | Thr192(*) | −7.5 | Phe 131 | −14.2 | 189% |
| 18 | Ile194(*) | −7.3 | Gln129 | −8.5 | 116% |
| 19 | Val534(*) | −6.0 | Asp82(−) | −4.7 | 78% |
| 20 | Tyr543(*) | −5.1 | Ser73 | −3.2 | 63% |
| Rank | (b) Nectin-4 (Chain B in PDB Code 4JGT) | ||||
| 1 | Arg547(+) | −46.4 | Glu2(−) | −42.1 | 91% |
| 2 | Ser550(*) | −29.5 | Asp26(−) | −25.8 | 87% |
| 3 | Gln391 | −27.5 | Tyr55 | −24.4 | 89% |
| 4 | Tyr543(*) | −16.8 | Gly104 | −5.8 | 35% |
| 5 | Thr392(*) | −16.8 | Lys 54(+) | −18.3 | 109% |
| 6 | Leu500(*) | −11.7 | Lys 54(+) | −6.3 | 54% |
| 7 | Leu464(*) | −10.9 | Thr100 | −6.1 | 56% |
| 8 | Phe483(*) | −10.0 | Ser105 | −5.3 | 53% |
| 9 | Gly506(*) | −9.3 | Gln 30 | −9.3 | 100% |
| 10 | Ser548(*) | −9.1 | Glu2(−) | −10.2 | 112% |
| 11 | Gly465(*) | −7.1 | Ala 103 | −11.7 | 165% |
| 12 | Gly388(*) | −6.3 | Tyr 55 | −4.6 | 73% |
| 13 | Tyr499(*) | −5.9 | Lys 54(+) | −5.6 | 95% |
| 14 | Tyr524(*) | −3.9 | Gly 104 | −2.9 | 74% |
| 15 | Lys460(+) | −3.1 | Phe101 | −3.1 | 100% |
| 16 | Val485(*) | −2.3 | Gln33 | −1.6 | 70% |
| 17 | Pro486 | −2.1 | Gln 33 | −1.7 | 81% |
| 18 | Ala463(*) | −1.9 | Phe 101 | −1.9 | 100% |
| 19 | Pro458 | −1.9 | Ala103 | −2.0 | 105% |
| 20 | Ile390(*) | −1.1 | Lys 54(+) | −1.1 | 100% |
| Rank | (c) CD46 (Chain D in PDB Code 3INB) | ||||
| 1 | Lys477(+) | −66.2 | Asp70(−) | −67.4 | 102% |
| 2 | Glu503(−) | −36.1 | Ala41 | −23.3 | 65% |
| 3 | Gly546(*) | −33.7 | Glu63(−) | −27.2 | 81% |
| 4 | Lys488(+) | −29.6 | Gly81 | −29.9 | 101% |
| 5 | Tyr481(*) | −22.1 | Pro66 | −14.5 | 66% |
| 6 | Glu471(−) | −17.9 | Arg69(+) | −51.4 | 287% |
| 7 | His448 | −14.2 | Arg69(+) | −10.0 | 70% |
| 8 | Pro501 | −7.3 | Asp58(−) | −5.6 | 77% |
| 9 | Phe483(*) | −6.6 | Tyr 61 | −3.7 | 56% |
| 10 | Pro486 | −6.4 | Thr 82 | −4.0 | 63% |
| 11 | Tyr543(*) | −6.3 | Ile37 | −15.5 | 246% |
| 12 | Arg547(+) | −6.3 | Glu63(−) | −45.4 | 721% |
| 13 | Thr498(*) | −6.2 | Tyr 61 | −6.2 | 100% |
| 14 | Val485(*) | −4.3 | Arg62(+) | −4.5 | 105% |
| 15 | Tyr541(*) | −4.3 | Pro38 | −1.7 | 40% |
| 16 | His495 | −3.6 | Thr 82 | −4.2 | 117% |
| 17 | Val451(*) | −3.4 | Tyr 67 | −1.8 | 53% |
| 18 | Pro545 | −3.3 | Glu63(−) | −1.9 | 58% |
| 19 | Thr469(*) | −2.2 | Tyr 67 | −2.2 | 100% |
| 20 | Leu462(*) | −2.1 | Pro39 | −1.5 | 71% |
(1) “MVH amino acid (a.a.) position” shows amino acid residues of MVH and their sequence number with electric charge (+ or −) or hydrophobicity (*) in the parentheses. Ranking of the MVH a.a. is descending from the highest (most attractive) IFIE value on the top to the lower IFIE values downward; (2) “IFIE sum” is the summation of the IFIE values with the residues of the receptor located within the pair distance of 5 Å; (3) “Receptor a.a. with the highest (1st) affinity” indicates the most attractive amino-acid residue of the receptor to the corresponding MVH residue on the same line. Its position is shown as the sequence number with its electric charge (+ or −) in the parentheses; (4) “IFIE-1st” is the IFIE between the designated MVH a.a. and the receptor a.a. with the highest (1st) affinity; (5) Contribution of the receptor a.a. with the highest (1st) affinity to the IFIE sum of the single MVH residue and the receptor residues was evaluated as a ratio between the IFIE-1st and the IFIE sum.